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Database: UniProt
Entry: A0A135TIL0_9PEZI
LinkDB: A0A135TIL0_9PEZI
Original site: A0A135TIL0_9PEZI 
ID   A0A135TIL0_9PEZI        Unreviewed;       517 AA.
AC   A0A135TIL0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Dimethylaniline monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CSAL01_07275 {ECO:0000313|EMBL:KXH47945.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH47945.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH47945.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH47945.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH47945.1}.
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DR   EMBL; JFFI01001962; KXH47945.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135TIL0; -.
DR   OrthoDB; 445965at2759; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
SQ   SEQUENCE   517 AA;  56880 MW;  E957656764161314 CRC64;
     MESQSKRVAV IGAGPSGLVA IKECLAAGLE VQCFERAPAL GGLWLYNPDP TAETSSGMYP
     GVMLNSCRLT TGYSDFPIDP ARYPIYYSHK LHLRYLNEYA AHFALEKHIR YETTVVGCAP
     RKDGGWEVRV RRGSAEDGRG EEVLVFDALI CGTGIISKPF IPEYKGREAF KGEVLHSRSY
     RKPSAYEGKK VVLVGLGSSA IDVACEVGPL AKELTIVNRR GAWILPRFVL GKPTEAWDSR
     SSQVWLPASV QEWLFEKILN HAQGKMPPEL QPDHGLMAQN ATLRSDFVEK LQTGIFSLRR
     TAIASFTETG VILENGDALD ADVVILATGY HIVDQPYLPP GALASKEAPA PHVDLYKSIV
     SPTWKDLYVM GQTEQAGPVT PVSEAQARFI AAVIKGSVKL PGEEEMMREI RMLRGWRKKH
     MIDSDRHALN VEFVKYMDGL LAPLGATPTF GKLFGRIFTS GKPLRAWSIL SAVYFGIPAP
     AQWRLFGEGS TPVLAEETLL RTDVDASQLS EGEKSFL
//
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